My laboratory uses genetically-modified human cell lines to study the way changes in cell adhesion proteins can contribute to tumor development.  We are specifically interested in the role of P-cadherin, a molecule located on the sides of cells that helps hold cells together to form tissues, and N-cadherin, which becomes abnormally expressed in epithelial cancers.   Current research efforts are focused on three areas in which cadherin expression may alter tumor development:

1.  P-cadherin-dependent tumor progression in non-small cell lung cancer. Clinical studies have suggested that P-cadherin decreases overall survival in patients with non-small cell lung cancer tumors that have abnormally high levels of P-cadherin expression.  We are using genetically-modified lung cancer cell lines to examine the mechanisms by which P-cadherin may promote tumor development and aggressiveness.
2. P-cadherin-dependent chemoresistance in Oral Squamous Cell Carcinoma. We have found that increased levels of P-cadherin can cause oral cells to exhibit either greater resistance or greater sensitivity to different classes of chemotheraputic drugs that are used to treat oral cancer.  We are currently using a proteomics (protein-based) approach to define the P-cadherin-driven signaling networks that play an important role in cell death vs. cell survival in cells treated with these agents.
3. Metabolic consequences of N-cadherin in oral squamous cell carcinoma. We are using both an oral precancer and oral squamous carcinoma model system to evaluate the effects of N-cadherin on metabolic signaling, including stimulation the Warburg effect to increase both glucose utilization and anaerobic glycolysis.

1. Lysne, D, Johns J, Walker, A, Ecker R, Fowler, C, & Lawson KR.  "P-cadherin potentiates ligand-dependent EGFR and IGF-1R signaling in dysplastic and malignant oral keratinocytes". Oncology Rep. (2014) 32(6): 2541-2548.

2. Walker, A, Frei, R, and Lawson K.  "The cytoplasmic domain of N-cadherin modulates MMP-9 induction in oral squamous carcinoma cells". Int J. Oncology. (2014) 45(4):1699- 1706.

3. Maeda, M., Johnson, E., Mandal, S.H., Lawson, K. R., Keim, S. A., Svoboda, R. A., Caplan, S., Wahl, J. K., Wheelock, M. J., and Johnson, K.R. “Expression of inappropriate cadherins by epithelial tumor cells promotes endocytosis and degradation of E-cadherin via competition for p120ctn.." Oncogene. (2006) 25(33):4595-4604.

4. Lawson K, Larentowicz L, Artim S, Hayes CS, Gilmour SK. “A novel protein kinase CK2 substrate indicates CK2 is not directly stimulated by polyamines in vivo.” Biochemistry. (2006) (5):1499-510.

5. Lawson, K., Larentowicz L, Laury-Kleintop, L., Gilmour, S.K. “B23 is a downstream target of polyamine-modulated CK2.” Mol Cell Biochem. (2005) 274(1-2):103-14.

American Association For Cancer Research (1996 - present)

American Society for Biochemistry and Moleculear Biology (2018-present)